Structure of PDB 9ldb Chain B

Receptor sequence
>9ldbB (length=331) Species: 9823 (Sus scrofa) [Search protein sequence]
ATLKDQLIHNLLKEEHVPHNKITVVGVGAVGMACAISILMKELADEIALV
DVMEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSRLVVITAGARQQ
EGESRLNLVQRNVNIFKFIIPNIVKYSPNCKLLVVSNPVDILTYVAWKIS
GFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWILGEHGDSSVPVW
SGVNVAGVSLKNLHPELGTDADKEHWKAVHKEVVDSAYEVIKLKGYTSWA
IGLSVADLAESIMKNLRRVHPISTMIKGLYGIKENVFLSVPCILGQNGIS
DVVKVTLTPEEEAHLKKSADTLWGIQKELQF
3D structure
PDB9ldb Design and synthesis of new enzymes based on the lactate dehydrogenase framework.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R109 D168 R171 H195
Catalytic site (residue number reindexed from 1) R105 D165 R168 H192
Enzyme Commision number 1.1.1.27: L-lactate dehydrogenase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD B G30 A31 V32 D53 V54 M55 T97 A98 G99 A100 R101 I119 V138 N140 H195 I250 G28 A29 V30 D51 V52 M53 T94 A95 G96 A97 R98 I115 V135 N137 H192 I251
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004459 L-lactate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0042802 identical protein binding
Biological Process
GO:0006089 lactate metabolic process
GO:0006090 pyruvate metabolic process
GO:0019752 carboxylic acid metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:1990204 oxidoreductase complex

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Cellular Component
External links
PDB RCSB:9ldb, PDBe:9ldb, PDBj:9ldb
PDBsum9ldb
PubMed1678537
UniProtP00339|LDHA_PIG L-lactate dehydrogenase A chain (Gene Name=LDHA)

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